Horseshoe Crab Hemocyte- Derived Lectin Recognizing Specific 0-Antigens of Lipopolysaccharides

Inamori, Kei-ichiro; Saito, Tetsu; Iwaki, Daisuke; Nagira, Tsutomu; Iwanaga, Sadaaki; Arisaka, Fumio; Kawabata, Shun-ichiro

doi:10.1007/978-1-4615-1291-2_16

Cited by 6 publications

(5 citation statements)

References 15 publications

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“…This crossreactivity was assumed to be attributable to molecular mimicry between Pnc carbohydrate antigens and blood group antigens [48]. Such molecular mimicry has been described most extensively for the lipopolysaccharides of Gram-negative gut pathogens such as Helicobacter pylori, which is considered to be a bacterial strategy to avoid host defence [49,50], although lectins have been described which function in much the same way as natural IgM, recognizing conformatory structures, specifically binding both blood group antigens and certain bacterial lipopolysaccharide O-antigens [51,52].…”

Section: Discussionmentioning

confidence: 99%

Natural human antibodies to pneumococcus have distinctive molecular characteristics and protect against pneumococcal disease

Baxendale¹,

Johnson²,

Stephens

et al. 2007

Clinical and Experimental Immunology

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SummaryThe molecular and functional characteristics of natural antibody from the preimmune repertoire have not been explored in detail in man. We describe seven human IgM monoclonal antibodies selected on the basis of pneumococcal polysaccharide binding that share both molecular and functional characteristics with natural antibody, suggesting a common B cell lineage origin. Unlike class-switched antibodies, which are serotype-specific, the antibodies were polyreactive and bound all pneumococcal polysaccharide capsular serotypes tested. Some bound endogenous antigens, including blood group antigens and intermediate filament proteins. All the antibodies used unmutated heavy chain V (IGHV) that are expressed at an increased frequency in the elderly and in the preimmune repertoire. The CDR3 was characterized by long length (mean aa 18·4 (Ϯ4·2) and selective use of IGHD6 (P < 0·001) and IGHJ6 (P < 0·01) family genes. The clones expressing IGHV1-69 and IGHV 3-21 provided significant passive protection against invasive pneumococcal disease in vivo.

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Section: Discussionmentioning

confidence: 99%

Natural human antibodies to pneumococcus have distinctive molecular characteristics and protect against pneumococcal disease

Baxendale¹,

Johnson²,

Stephens

et al. 2007

Clinical and Experimental Immunology

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“…In view of the fact that a series of antimicrobial lectins exist in another arthropod, the horseshoe crab (Gokudan et al ., 1999; Inamori et al ., 2001), it might be predicted that such a diversity occurs in insects. To date, more than forty gene products containing FBG domains have been annotated in the An.…”

Section: Discussionmentioning

confidence: 99%

A novel lectin with a fibrinogen‐like domain and its potential involvement in the innate immune response of Armigeres subalbatus against bacteria

Wang

Rocheleau

Fuchs

et al. 2004

Insect Molecular Biology

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Mosquitoes have an efficient cellular innate immune response that includes phagocytosis of microbial pathogens and encapsulation of metozoan parasites. In this study, we describe a novel lectin in the mosquito, Armigeres subalbatus (aslectin or AL-1). The 1.27 kb cDNA clone for the AL-1 gene (AL-1) encodes a 279 deduced amino acid sequence that contains a C-terminal fibrinogen-like domain. AL-1 is transcribed in all life stages. AL-1 mainly exists in the haemolymph of adult female mosquitoes, and is upregulated following both Escherichia coli and Micrococcus luteus challenge. AL-1 specifically recognizes N-acetyl-d-glucosamine and is able to bind both E. coli and M. luteus. These results suggest that AL-1 might function as a pattern recognition receptor in the immune response in Ar. subalbatus.

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“…On the other hand TPL-2 which is also found in plasma shows ligand specificity toward LPS, particularly O-antigen. TL-3 (a homologue of TPL-2) was also identified as recognizing the O-antigen of LPS with comparable activity (MIC = 0.01 mM) [20]. However, TL-3 is a non-glycosylated lectin located in amaebocytes and it does not require intermolecular disulphide bonds for activity.…”

Section: Detection Of Bacteria By Tpl-1 and Tpl-2mentioning

confidence: 99%

Ligand specificities and structural requirements of two Tachypleus plasma lectins for bacterial trapping

Kuo

Chuang

Chang

et al. 2006

Biochemical Journal

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TPL (Tachypleus plasma lectin)-1 was purified by using a Sepharose column and TPL-2 was purified from an LPS-Sepharose (LPS coupled to Sepharose matrix) affinity column, as described previously [Chiou, Chen, Y.-W., Chen, S.-C., Chao and Liu (2000) J. Biol. Chem. 275, 1630-1634] and the corresponding genes were cloned [Chen, Yen, Yeh, Huang and Liu (2001) J. Biol. Chem. 276, 9631-9639]. In the present study, TPL-1 and -2 were produced in yeast, and the recombinant proteins secreted into the media were purified and characterized. The proteins show specific PGN (peptidoglycan)- and LPS-binding activity, suggesting a role in trapping Gram-positive and Gram-negative bacteria respectively in innate immunity. Using BIAcore assays, the dissociation constant for the TPL-1-PGN complex was measured as 8x10(-8) M. Replacement of Asn74, the N-glycosylation site of TPL-1, with Asp abolishes the PGN-binding affinity, whereas the unglycosylated TPL-2 N3D mutant retains LPS-binding activity. DTT (dithiothreitol) treatment to break disulphide linkages abrogates TPL-2 activity but does not interfere with TPL-1 function. Cys4 in TPL-2 may form an intermolecular disulphide bond, which is essential for activity. As a result, the TPL-2 C4S mutant is inactive and is eluted as a monomer on a non-reducing gel. TPL-2 C6S is active and forms a non-covalently linked dimer. A model describing TPL-2 binding with LPS is proposed. These two plasma lectins that have different ligand specificities can be used for the detection and discrimination of bacteria and removal of endotoxins.

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Horseshoe Crab Hemocyte- Derived Lectin Recognizing Specific 0-Antigens of Lipopolysaccharides

Cited by 6 publications

References 15 publications

Natural human antibodies to pneumococcus have distinctive molecular characteristics and protect against pneumococcal disease

Natural human antibodies to pneumococcus have distinctive molecular characteristics and protect against pneumococcal disease

A novel lectin with a fibrinogen‐like domain and its potential involvement in the innate immune response of Armigeres subalbatus against bacteria

Ligand specificities and structural requirements of two Tachypleus plasma lectins for bacterial trapping

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